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Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein
Abstract
Alpha-synuclein (alpha-syn) and tau polymerize into amyloid fibrils and form intraneuronal filamentous inclusions characteristic of neurodegenerative diseases. We demonstrate that alpha-syn induces fibrillization of tau and that coincubation of tau and alpha-syn synergistically promotes fibrillization of both proteins. The in vivo relevance of these findings is grounded in the co-occurrence of alpha-syn and tau filamentous amyloid inclusions in humans, in single transgenic mice that express A53T human alpha-syn in neurons, and in oligodendrocytes of bigenic mice that express wild-type human alpha-syn plus P301L mutant tau. This suggests that interactions between alpha-syn and tau can promote their fibrillization and drive the formation of pathological inclusions in human neurodegenerative diseases.
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“Evidence suggests that Aβ can directly affect α-synuclein toxicity, and it is also known that tau protein and α-synuclein can directly interact promoting their co-assembly [124–126].”
From The neuropathological diagnosis of Alzheimer's disease (2019) · cites this paper as [125]
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BackgroundCystatin A, a Potential Common Link for Mutant Myocilin Causative Glaucoma
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Yeast prion protein New1 can break Sup35 amyloid fibrils into fragments in an ATP-dependent manner
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“Paradoxically, accumulating evidences have shown that the transmission of amyloid across nonrelated proteins can occur (Giasson et al. 2003; Fu et al. 2004; O’Nuallain et al. 2004), including the cases of yeast prion proteins (Derkatch et al. 2004; Vitrenko et al. 2007).”
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“Cross-seeding experiments further demonstrated that an aggregate nucleus of one protein can induce fibril formation of an unrelated protein.(4,8) Whether cross-seeding occurs in vivo is unclear, however the co-occurrence of distinct protein aggregates indicates the possibility that additional proteins are triggered by…”
BackgroundLack of exacerbation of neurodegeneration in a double transgenic mouse model of mutant LRRK2 and tau
Mikhail, F., Calingasan, N. Y., Parolari, L., Subramanian, A., Yang, L., & Beal, M. F. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv105 · Cited by 23
“vice versa, and there is often considerable co-staining of tau with α-synuclein in PD brains (53).”
BackgroundThe role of annealing and fragmentation in human tau aggregation dynamics
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Photodynamic studies reveal rapid formation and appreciable turnover of tau inclusions
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“In brief, the cDNA corresponding to the human tau K18 fragment (residues Q244-E372 in 2N/4R human tau) with an added methionine residue at the N-terminus cloned in the bacterial expression plasmid pRK172 was expressed in BL21 (DE3)/RIL Escherichia coli (Agilent Technologies, Santa Clara, CA, USA) and was purified as p…”
MethodSelf-citationStability of Amyloid Oligomers
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Cross-talk between α-synuclein and the microtubule cytoskeleton in neurodegeneration
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“To note, α-synuclein and tau synergically promote the mutual polymerization into fibrils in multiple animal models including transgenic mice expressing A53T human α-synuclein and bigenic mice expressing wildtype human α-synuclein plus P301L mutant tau (Giasson et al., 2003).”
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Majd, S., Chegini, F., Chataway, T., Zhou, X., & Gai, W. (2012) · Neurotoxicity Research · doi:10.1007/s12640-012-9330-y · Cited by 22
“Thus, high concentrations of Ab1-42 and a-Syn exert toxic effects on mature neurons; however, non-toxic concentration treat- ment of these polypeptides induced the production of each other reciprocally with possible involvement of PI3K pathway.”
BackgroundSilveira‐Moriyama, L., Gonzalez, A. M. D., O’Sullivan, S. S., Williams, D. R., Massey, L. A., Parkkinen, L., Ahmed, Z., de Silva, R., Chacón, J., Révész, T., et al. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.10.036 · Cited by 22
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Tau protein, the main component of paired helical filaments
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“Later on, several groups described other components like polyanions [33], fatty acids [34,35], or some or their oxidized products [36,37], quinones [38], proteins likeα-synuclein [39], or 14-3-3 [40], solvents like TFE [41] or others [42] that facilitate tau polymerization.”
Magic-Angle-Spinning Solid-State NMR Applied to Polypeptides and Proteins
Hughes, C. E., & Baldus, M. (2005) · Annual reports on NMR spectroscopy · doi:10.1016/s0066-4103(04)55002-0 · Cited by 22
Parkinson's disease: From genetics to molecular dysfunction and targeted therapeutic approaches
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“The Cterminus of a-synuclein interacts with the microtubule binding domain of tau, particularly when tau is hyperphosphorylated,(25) and facilitates the formation of neuropathological intraneuronal filamentous inclusinons.(26,27) Molecular functions of a-synuclein provide further pathophysiological evidence about the…”
BackgroundAmyloid Protein Cross-Seeding Provides a New Perspective on Multiple Diseases In Vivo
Ge, W., Deng, X., Shi, W., Lin, W.-J., Chen, L., Liang, H., Wang, X., Zhang, T., Zhao, F., Guo, W., et al. (2022) · Biomacromolecules · doi:10.1021/acs.biomac.2c01233 · Cited by 24
Different MAPT haplotypes influence expression of total MAPT in postmortem brain tissue
Tauber, C. V. I., Schwarz, S. C., Rösler, T. W., Arzberger, T., Gentleman, S., Windl, O., Krumbiegel, M., Reis, A., Ruf, V., Herms, J. W., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01534-9 · Cited by 21
“In vitro studies demonstrated that tau and α-syn can mutually promote each others aggregation [19, 20].”
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A systematic review of salivary biomarkers in Parkinson’s disease
Bartolo, M. I. D., Belvisi, D., Mancinelli, R., Costanzo, M., Caturano, C., Leodori, G., Berardelli, A., Fabbrini, G., & Vivacqua, G. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01677 · Cited by 21
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Kang, J. (2016) · Journal of Movement Disorders · doi:10.14802/jmd.16017 · Cited by 21
14-3-3ζ Mediates Tau Aggregation in Human Neuroblastoma M17 Cells
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“The pellet is suspended in the buffer and then centrifuged, and the insoluble tau that remains in the pellet is regarded as the aggregated form [15, 32].”
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“…disease and that both tau and a-synuclein synergistically effect the polymerization of each other into fibrillar amyloid lesions, which provides insight into mechanisms that underlie the formation of pathological inclusions found in both Parkinson’s and Alzheimer’s disease (Giasson et al., 2003).”
BackgroundEvaluation of the Common Molecular Basis in Alzheimer’s and Parkinson’s Diseases
Rana, P., Franco, E. F., Rao, Y., Syed, K., Barh, D., Azevedo, V., Ramos, R. T. J., & Ghosh, P. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20153730 · Cited by 22
“The toxic interaction between tau and α-synuclein may lead to the deposition of both proteins in the brain [60].”
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Dementia with Lewy Bodies: Current Concepts
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“a-Synuclein is also associated with other disorders such as multiple system atrophy and REM behavior disorder, which suggests that DLB is part of a larger group of disorders that have come to be known as ‘synucleinopathies’. a-Synuclein pathologic lesions have also been found to colocalize with tau lesions in diseases…”
BackgroundNeurofibrillary tau pathology modulated by genetic variation of α‐synuclein
Peuralinna, T., Oinas, M., Polvikoski, T. M., Paetau, A. E., Sulkava, R. O., Niinistö, L., Kalimo, H., Hernandez, D. G., Hardy, J., Singleton, A., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21446 · Cited by 21
“Previously, tau and -synuclein have been shown to interact at the protein level, and they can seed each other’s aggregation at low protein concentrations.(18) Two recent genetic studies have suggested that SNCA alleles and MAPT haplotype H1 homozygosity may have an interactive effect on PD risk.”
BackgroundCross-Species and Cross-Polymorph Seeding of Lysozyme Amyloid Reveals a Dominant Polymorph
Araghi, L. R., & Dee, D. R. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00206 · Cited by 22
Lewy Body Dementias: A Coin with Two Sides?
Milán-Tomás, Á., Fernández‐Matarrubia, M., & Rodríguez-Oroz, M. C. (2021) · Behavioral Sciences · doi:10.3390/bs11070094 · Cited by 24
“From both clinical and pathological perspectives, LBDs are heterogeneous disorders, and different studies indicate that the cognitive decline and related symptoms are not only a consequence of α-syn induced neurodegeneration, but also of mixed pathologies contributing to the overall deficits [68,69,71,82,83].”
BackgroundRoles of α-Synuclein and Disease-Associated Factors in Drosophila Models of Parkinson’s Disease
Suzuki, M., Sango, K., & Nagai, Y. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031519 · Cited by 20
“Biochemical analyses also strengthened this link; Giasson and coworkers reported that αSyn induces the fibrillization of Tau, and that the coincubation of Tau and αSyn synergistically promotes the fibrillization of both proteins [118].”
BackgroundSchreiber, C. S., Wiesweg, I., Stanelle‐Bertram, S., Beck, S., Kouassi, N. M., Schaumburg, B., Gabriel, G., Richter, F., & Käufer, C. (2024) · EBioMedicine · doi:10.1016/j.ebiom.2024.105191 · Cited by 21
“29,30 Its deposits can be found in several neurodegenerative diseases, together termed synucleinopathies, including Parkinson ’ s Disease (PD).”
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“DISCUSSION >-SynucleinYpositive pathology has been identified in a variety of disorders with extensive tau pathology including sporadic Alzheimer disease (13, 14), familial Alzheimer disease (15), DLB (16), familial DLB (17), familial Parkinson disease associated with the >-synuclein A53T mutation (18), Down syndrome…”
BackgroundRole of FK506 Binding Proteins in Neurodegenerative Disorders
Chattopadhaya, S., Harikishore, A., & Yoon, H. S. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711798194441 · Cited by 20
“The relevance of tau in PD pathogenesis stems from the observations that (1) it accumulates in LBs together with -SYN [107]; (2) analysis of synapse-enriched fractions from PD brains showed an increase in phosphorylation for both tau and -SYN [108] and (3) in vitro studies have indicated that tau and SYN synergistical…”
BackgroundNeurodegenerative Diseases and Ageing
Walker, L., McAleese, K. E., Erskine, D., & Attems, J. (2019) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-13-3681-2_4 · Cited by 21
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How much does dardarin contribute to Parkinson's disease?
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Animal modeling an oligodendrogliopathy – multiple system atrophy
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“A number of microtubule-interacting proteins have been implicated in α-synuclein aggregation or are found colocalized with α-synuclein in pathological aggregates in both MSA and PD, including tubulin [69], p25α [70] and tau [71].”
BackgroundTargeting tau in Alzheimer’s and beyond: Insights into pathology and therapeutic strategies
Singh, S., Khan, S., Shahid, M., Sardar, M., Hassan, M. I., & Islam, A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102639 · Cited by 19
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“This is one of the possible mechanisms by which one disease aggravates the other disease such as Alzheimer’s disease together with either Type 2 diabetes (Bharadwaj et al., 2017; Biessels et al., 2005 or Parkinson’s disease Guo et al., 2013; Giasson et al., 2003).”
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“With tau and alphasynuclein being the two most important genetic risk factors of Parkinson’s disease (PD) [56] and in view of the co-precipitation of these two proteins in the pathognomonic cytoplasmic “Lewy body” inclusions [57, 58], it is interesting that we found an upregulation of glyoxalase I to be the prominent…”
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“Aggregation of alpha-synuclein characteristic for PD is stimulated by tubulin, tau and TPPP=p25 [Giasson et al., 2003; Lindersson et al., 2005; Kim et al., 2008].”
BackgroundThe role of α-synuclein in neurodegeneration — An update
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“Animal models and in vitro studies have shown that Aß, tau, and a-synuclein mutually promote their accumulation, thus providing a partial explanation for the simultaneous presence of different neuropathological features in the same subject.(53,54) This also suggests the possibility of onset, during aging, of different…”
BackgroundShi, C., Zheng, Z., Wang, Q., Wang, C., Zhang, D., Zhang, M., Chan, P., & Wang, X. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155758 · Cited by 19
Recent advances in experimental modeling of the assembly of tau filaments
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“[74] B.”
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Does essential tremor increase risk of cognitive impairment and dementia? Yes
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The molecular spectrum of amyloid‐beta (Aβ) in neurodegenerative diseases beyond Alzheimer's disease
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A computational study of self-assembled hexapeptide inhibitors against amyloid-β (Aβ) aggregation
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Novel approach for accurate tissue-based protein colocalization and proximity microscopy
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Formation of Heterotypic Amyloids: α‐Synuclein in Co‐Aggregation
Bhasne, K., & Mukhopadhyay, S. (2018) · PROTEOMICS · doi:10.1002/pmic.201800059 · Cited by 17
A role of cellular translation regulation associated with toxic Huntingtin protein
Joag, H., Ghatpande, V., Desai, M., Sarkar, M., Raina, A., Shinde, M., Chitale, R., Deo, A., Bose, T., & Majumdar, A. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03392-y · Cited by 15
Santos-Rebouças, C. B., Abdalla, C. B., Baldi, F. J. R., Martins, P. Á., Corrêa, J. C., Gonçalves, A. P., Cunha, M. S., de Borges, M. B., Pereira, J. S., Laks, J., et al. (2008) · Genetic Testing · doi:10.1089/gte.2008.0042 · Cited by 18
“…the hallmarks of AD and PD, respectively, has also shared common mechanisms. a - Synuclein has been shown to induce the in vitro formation of tau fibrils, and both tau and a -synuclein synergistically promote the polymerization of each other into fibrillar amyloid lesions (Giasson et al. , 2003).”
Windisch, M., Hutter‐Paier, B., Schreiner, E., & Wronski, R. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:24:1:155 · Cited by 18
Interactions of Volatile Anesthetics with Neurodegenerative-Disease-Associated Proteins
Carnini, A., Eckenhoff, M. F., & Eckenhoff, R. G. (2006) · Anesthesiology Clinics of North America · doi:10.1016/j.atc.2006.02.002 · Cited by 18
“Recent studies have found that amyloid b stimulates tau and a-synuclein pathology [52,53] and that a-synuclein stimulates tau pathology [54–56].”
BackgroundConcomitant protein pathogenesis in Parkinson’s disease and perspective mechanisms
Han, Y., & He, Z. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1189809 · Cited by 18
“Moreover, α-synuclein has been also shown to induce tau aggregation in a process termed cross-seeding (Giasson et al., 2003; Guo et al., 2013; Bassil et al., 2020).”
BackgroundInfluentialBeyond Strains: Molecular Diversity in Alpha-Synuclein at the Center of Disease Heterogeneity
Wojewska, M. J., Otero‐Jimenez, M., Guijarro-Nuez, J., & Alegre‐Abarrategui, J. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713199 · Cited by 19
Interaction of Proteins Involved in Neuronal Proteinopathies
Kulichikhin, K. Y., Malikova, O. A., Zobnina, A. E., Zalutskaya, N. M., & Rubel, A. A. (2023) · Life · doi:10.3390/life13101954 · Cited by 17
Gawor, K., Tomé, S. O., Vandenberghe, R. R., Damme, P. V., Vandenbulcke, M., Otto, M., Arnim, C. A. F. V., Ghebremedhin, E., Ronisz, A., Ospitalieri, S., et al. (2024) · Brain Communications · doi:10.1093/braincomms/fcae442 · Cited by 22
“97 Previous studies using animal and cell models have demonstrated that α Syn aggregates can induce the fibril-lization and aggregation of tau 49,53,78,79 and TDP-43.”
Screening non-MAPT genes of the Chr17q21 H1 haplotype in Parkinson's disease
Soto‐Beasley, A. I., Walton, R. L., Valentino, R. R., Hook, P. W., Labbé, C., Heckman, M. G., Johnson, P. W., Goff, L. A., Uitti, R. J., McLean, P. J., et al. (2020) · Parkinsonism & Related Disorders · doi:10.1016/j.parkreldis.2020.07.022 · Cited by 17
Adem, K. A., Shanti, A., Srivastava, A., Homouz, D., Thomas, S. A., Khair, M., Stefanini, C., Chan, V., Kim, T., & Lee, S. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.842582 · Cited by 17
“In addition to IAPP and Aβ40 co-aggregation, the co-aggregation of other proteins such as Tau and α-Synuclein (Giasson, 2003), IAPP and α-Synuclein (Horvath and Wittung-Stafshede, 2016), IAPP and Tau-Fragment R3 (Arya et al., 2019), Aβ and α-Synuclein (Luo et al., 2016; Bhasne andMukhopadhyay,…”
BackgroundInteraction between α-Synuclein and Tau Genotypes and the Progression of Parkinson's Disease
Huang, Y. M., Rowe, D. B., & Halliday, G. M. (2011) · Journal of Parkinson s Disease · doi:10.3233/jpd-2011-11027 · Cited by 17
“At low concentrations of the (cid:1) -synuclein protein microtubule-associated protein tau [15] with high tau gene expression (H1H1 genotype) possibly conferring increased PD risk in the relatively low -synuclein expressors (non-+1/+1 genotype) [16].”
Refenes, N., Bolbrinker, J., Tagaris, G. L., Orlacchio, A., Drakoulis, N., & Kreutz, R. H. (2009) · BMC Neurology · doi:10.1186/1471-2377-9-26 · Cited by 17
“In addition, a disease mechanism based on the protein tau has been proposed in PD [5,6].”
BackgroundRecent advances in our understanding of Parkinson's disease
Kim, S. W., Ko, H. S., Dawson, V. L., & Dawson, T. M. (2005) · Drug Discovery Today Disease Mechanisms · doi:10.1016/j.ddmec.2005.11.015 · Cited by 17
Trends in glycolipid biomarker discovery in neurodegenerative disorders by mass spectrometry
Dehelean, L., Sarbu, M., Petrut, A., & Zamfir, A. D. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-15950-4_42 · Cited by 16
Gao, R., Zhang, G., Chen, X., Yang, A., Smith, G. S., Wong, D. F., & Zhou, Y. (2016) · PLoS ONE · doi:10.1371/journal.pone.0164762 · Cited by 17
Novel monoclonal antibodies targeting the microtubule-binding domain of human tau
Croft, C. L., Moore, B. D., Ran, Y., Chakrabarty, P., Levites, Y., Golde, T. E., & Giasson, B. I. (2018) · PLoS ONE · doi:10.1371/journal.pone.0195211 · Cited by 16
Self-citationLipid metabolism in Alzheimer’s and Parkinson’s disease
Xu, Q., & Huang, Y. (2006) · Future Lipidology · doi:10.2217/17460875.1.4.441 · Cited by 16
Mechanisms and models of α-synuclein-related neurodegeneration
Springer, W., & Kahle, P. J. (2006) · Current Neurology and Neuroscience Reports · doi:10.1007/s11910-996-0025-8 · Cited by 16
Neubauer, A., Weissenbrunner, D., Pekrun, S., Roeber, S., Ruf, V. C., Feyen, P. L. C., Strübing, F., & Herms, J. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02952-w · Cited by 17
“On a molecular level, there is evidence for α-syn inducing hyperphosphorylation and fibrillization of tau [32, 55].”
Jimenez-Harrison, D., Huseby, C. J., Hoffman, C. N., Sher, S., Snyder, D. T., Seal, B., Yuan, C., Fu, H., Wysocki, V. H., Giorgini, F., et al. (2023) · Biochemistry · doi:10.1021/acs.biochem.2c00581 · Cited by 16
Jellinger, K. A. (2023) · Journal of Neural Transmission · doi:10.1007/s00702-023-02660-3 · Cited by 17
Ashique, S., Kumar, N., Mishra, N., Muthu, S., Rajendran, R. L., Chandrasekaran, B., Obeng, B. F., Hong, C. M., Krishnan, A., Ahn, B., et al. (2024) · Pathology - Research and Practice · doi:10.1016/j.prp.2024.155451 · Cited by 16
Maarouf, C. L., Beach, T. G., Adler, C. H., Malek‐Ahmadi, M. H., Kokjohn, T. A., Dugger, B. N., Walker, D. G., Shill, H. A., Jacobson, S. A., Sabbagh, M. N., et al. (2013) · Biomarker Insights · doi:10.4137/bmi.s11422 · Cited by 15
A Systems Model of Parkinson's Disease Using Biochemical Systems Theory
Sasidharakurup, H., Melethadathil, N., Nair, B. G., & Diwakar, S. (2017) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2017.0056 · Cited by 15
Takamatsu, Y., Fujita, M., Ho, G. J., Wada, R., Sugama, S., Takenouchi, T., Waragai, M., Masliah, E., & Hashimoto, M. (2018) · Parkinson s Disease · doi:10.1155/2018/5789424 · Cited by 15
“Because αS pathology is promoted by other APs, such as Aβ [29] and tau [30], it is likely that evolvability of these molecules might also positively affect the evolvability of αS (Figure 2).”
BackgroundAstrocyte-Derived Exosomes in an iPSC Model of Bipolar Disorder
Attili, D., Schill, D. J., DeLong, C. J., Lim, K. C., Jiang, G., Campbell, K. F., Walker, K. A., Laszczyk, A. M., McInnis, M. G., & O’Shea, K. S. (2020) · Advances in neurobiology · doi:10.1007/978-3-030-45493-7_8 · Cited by 15
A new MAP-Rasagiline conjugate reduces α-synuclein inclusion formation in a cell model
Vale, N., Alves, C., Sharma, V., Lázaro, D. F., Silva, S., Gomes, P. A. C., & Outeiro, T. F. (2020) · Pharmacological Reports · doi:10.1007/s43440-019-00032-x · Cited by 15
Gentile, A., Amadoro, G., Corsetti, V., Ciotti, M. T., Serafino, A., & Calissano, P. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-13205 · Cited by 15
“…govern its aggregation state, such as an increase in concentration (i.e., by tripli-cation) [16–18], an inappropriate interaction with tau proteins [23], a post-translational phosphorylation at Ser 129 [24–26], an inappropriate cleavage of negatively charged C terminus [27–30], or oxidation and…”
Concomitant accumulation of α-synuclein and TDP-43 in a patient with corticobasal degeneration
Yamashita, S., Sakashita, N., Yamashita, T., Tawara, N., Tasaki, M., Kawakami, K., Komohara, Y., Fujiwara, Y., Kamikawa, M., Nakagawa, T., et al. (2014) · Journal of Neurology · doi:10.1007/s00415-014-7491-8 · Cited by 16
“asynuclein aggregation could be greatly enhanced upon coincubation with tau in a concentration-dependent manner in vitro [18].”
BackgroundMultiple pathologies in a patient with a progressive neurodegenerative syndrome
Liang, T.-W. (2005) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp.2004.039479 · Cited by 15
“Moreover, recent studies suggest that in vitro tau fibrillisation is initiated by and dependent upon the presence of α-synuclein.”
BackgroundSchreiber, C. S., Ramil, L. N., Bieligk, J., Meineke, R., Rimmelzwaan, G. F., Käufer, C., & Richter, F. (2025) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2025.05.021 · Cited by 15
Lv, Y., Ding, X.-S., Gao, L., Han, Z., Feng, C., Li, Y.-N., Wang, Y., Yang, Q., Simon, D. K., Wang, X., et al. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102995 · Cited by 17
Cross-seeding by prion protein inactivates TDP-43
Polido, S. A., Stuani, C., Voigt, A., Banik, P., Kamps, J., Bader, V., Grover, P. L., Krause, L. J., Zerr, I., Matschke, J., et al. (2023) · Brain · doi:10.1093/brain/awad289 · Cited by 15
AmyloComp: A Bioinformatic Tool for Prediction of Amyloid Co-aggregation
Bondarev, S. A., Uspenskaya, M. V., Leclercq, J. Y., Falgarone, T., Zhouravleva, G. A., & Kajava, A. V. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168437 · Cited by 14
Echávarri, C., Caballero, M. C., Aramendía, A., García‐Bragado, F., & Tuñón, T. (2011) · The Anatomical Record · doi:10.1002/ar.21413 · Cited by 13
“There is evidence that tau and a-synuclein can promote each other’s fibrillization in vitro and in vivo (Wirths et al., 2000; Giasson et al., 2003; Popescu et al., 2004; Clinton et al., 2010) and that the misfolding and aggregation of a disease protein may disrupt normal cellular mechanisms,…”
Background
Metadata
- Authors
- Giasson, B. I., Forman, M. S., Higuchi, M., Golbe, L. I., Graves, C. L., Kotzbauer, P. T., Trojanowski, J. Q., & Lee, V. M.-Y.
- Affiliations
- University of Medicine and Dentistry of New Jersey (US)
- Corresponding author
- Lee, Virginia M.-Y.
- ORCID
- Venue
- Science
- Published
- 2003-04-25
- Volume
- 300
- Issue
- 5619
- Pages
- 636-640
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2073893553
- Cited by
- 879
- References
- 27
- Citations by year
- 2026: 23 · 2025: 29 · 2024: 37 · 2023: 35 · 2022: 58 · 2021: 32 · 2020: 50 · 2019: 52 · 2018: 49 · 2017: 42 · 2016: 35 · 2015: 31 · 2014: 39 · 2013: 42 · 2012: 33
- FWCI
- 26.70
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- alpha-synuclein, tau protein, amyloid fibril formation, protein aggregation, neurodegenerative diseases, synucleinopathies, tauopathy, oligodendrocytes, P301L tau, A53T alpha-synuclein, transgenic mouse model, intraneuronal inclusions
- MeSH terms
- Amyloid, Animals, Biopolymers, Brain Chemistry, Humans, Mice, Inbred C3H, Mice, Inbred C57BL, Mice, Transgenic, Microscopy, Electron, Microscopy, Fluorescence, Nerve Tissue Proteins, Neurons, Oligodendroglia, Protein Conformation, Microscopy, Immunoelectron, tau Proteins, Neurodegenerative Diseases, Protein Isoforms, Tauopathies, Mice, Synucleins, alpha-Synuclein
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